{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nSLC23A1 encodes the sodium‐dependent vitamin C transporter 1 (SVCT1), a high‐capacity, sodium‐coupled carrier that is essential for the uptake of L‐ascorbic acid (vitamin C) from the diet. SVCT1 is principally expressed in polarized epithelial cells—including intestinal enterocytes, renal proximal tubule cells, hepatocytes, epidermal keratinocytes, and ocular tissues—where it localizes predominantly to the apical membrane to mediate vectorial transport. Functional analyses in models such as CaCo‑2 cells and Xenopus oocytes have demonstrated that SVCT1 exhibits saturable, Na⁺‑dependent vitamin C uptake with a substrate affinity (K₀.₅ around 70 µM) and a stoichiometry of approximately 2 Na⁺ per ascorbate molecule, ensuring efficient absorption and maintenance of whole‐body vitamin C homeostasis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "8"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nA complex network of regulatory and trafficking mechanisms modulates SVCT1 function. Post‐translational modifications such as N‑glycosylation have been shown to be critical for proper folding, stability, and apical membrane targeting; indeed, mutagenesis studies have revealed that loss of key glycosylation sites drastically impairs transporter expression and activity. Furthermore, discrete intracellular targeting signals present in the cytoplasmic N‑ and C‑termini, along with interactions with regulatory proteins such as Rab8a and glyoxylate reductase/hydroxypyruvate reductase (hGR/HPR), are fundamental for SVCT1 sorting and retention at the apical membrane. In addition, transcriptional control by factors including hepatic nuclear factors and adaptive responses to vitamin C deprivation—as well as post‐transcriptional modulation via microRNAs—further refine its expression in tissues such as liver, kidney, and even in response to oxidative stress. Genetic studies have also revealed that polymorphisms in SLC23A1 (and in related genes) can influence transporter function and ultimately vitamin C bioavailability in clinical conditions ranging from inflammatory bowel disease to periodontitis and preeclampsia."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "9", "end_ref": "23"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nRecent structural and functional insights further illuminate the molecular underpinnings of SVCT1‐mediated transport. Cryo–electron microscopy studies have provided high‐resolution structures that detail the vitamin C binding mode and the coordination of two sodium ions necessary for substrate translocation. Intriguingly, SVCT1 has been shown to possess dual substrate specificity by also transporting urate, thereby expanding its physiological relevance beyond vitamin C homeostasis. These discoveries, alongside genetic association studies linking SLC23A1 variants with altered transporter activity and disease susceptibility—including preeclampsia and disorders of the kidney—are paving the way for novel therapeutic strategies aimed at modulating vitamin C uptake."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "24", "end_ref": "26"}]}, {"type": "t", "text": ""}]}]}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Nancy P Maulén, Esther A Henríquez, Sybille Kempe, et al. 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